Fig. 2: Self-activation of lipase by aggregation in organic solvents. | Nature Communications

Fig. 2: Self-activation of lipase by aggregation in organic solvents.

From: An aggregation-induced conformation locking strategy facilitates the activation of lipase biocatalyst

Fig. 2

The transmittance (a) and the relatively catalytic activity (b) of Lipase TL in different content of organic solvents. p-Nitrophenyl butyrate (p-NPB) was used as the ester substrate for the activity assay. Error bars = standard deviation (SD); Data were presented as mean values ± SD (n = 3; n presents the sample size used to derive statistics). Source data are provided as a Source Data file. c Fluorescence spectra of 80% (v/v) organic solvents-induced Lipase TL aggregate dispersed in buffer solution (1 mg/mL). Excitation at 280 nm. d The simulated Lipase TL aggregate in n-propanol solution. For clarity, the n-propanol molecules were omitted. In the Lipase TL molecule, the peptide chain of the lid was highlighted in orange, while the tryptophan fluorescent was highlighted in yellow. The original Lipase TL structure is available in the Protein Data Bank under the accession number PDB 1DT3. e The snapshot of the lid domain structures of the native Lipase TL and the aggregated Lipase TL based on MD simulation. In the Ser-His-Asp catalytic triad, the red, gray, and blue represented the O, C, and N atoms, respectively.

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